GLYC_MOUSE
ID GLYC_MOUSE Reviewed; 478 AA.
AC P50431; Q64508; Q8R0X9;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Serine hydroxymethyltransferase, cytosolic;
DE Short=SHMT;
DE EC=2.1.2.1 {ECO:0000250|UniProtKB:P34896};
DE AltName: Full=Glycine hydroxymethyltransferase;
DE AltName: Full=Serine methylase;
GN Name=Shmt1; Synonyms=Shmt;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) IN
RP COMPLEX WITH PYRIDOXAL PHOSPHATE AND SUBSTRATES, COFACTOR, AND SUBUNIT.
RC STRAIN=129/Sv; TISSUE=Liver;
RX PubMed=11063567; DOI=10.1021/bi000635a;
RA Szebenyi D.M.E., Liu X., Kriksunov I.A., Stover P.J., Thiel D.J.;
RT "Structure of a murine cytoplasmic serine hydroxymethyltransferase
RT quinonoid ternary complex: evidence for asymmetric obligate dimers.";
RL Biochemistry 39:13313-13323(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Liver;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-316.
RX PubMed=8863732; DOI=10.1016/0378-1119(96)00391-5;
RA Nakshatri H., Bouillet P., Bhat-Nakshatri P., Chambon P.;
RT "Isolation of retinoic acid-repressed genes from P19 embryonal carcinoma
RT cells.";
RL Gene 174:79-84(1996).
RN [5]
RP PROTEIN SEQUENCE OF 22-32; 40-53; 331-342 AND 452-460, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Kidney, Liver, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Interconversion of serine and glycine.
CC {ECO:0000250|UniProtKB:P34896}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + glycine + H2O =
CC (6S)-5,6,7,8-tetrahydrofolate + L-serine; Xref=Rhea:RHEA:15481,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15636, ChEBI:CHEBI:33384,
CC ChEBI:CHEBI:57305, ChEBI:CHEBI:57453; EC=2.1.2.1;
CC Evidence={ECO:0000250|UniProtKB:P34896};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:11063567};
CC -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion.
CC {ECO:0000250|UniProtKB:P34896}.
CC -!- SUBUNIT: Homotetramer (PubMed:11063567). Identified in complex with
CC FAM175B and the other subunits of the BRISC complex, at least composed
CC of FAM175B/ABRO1, BRCC3/BRCC36, BABAM2 and BABAM1/NBA1.
CC {ECO:0000250|UniProtKB:P34896, ECO:0000269|PubMed:11063567}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- MISCELLANEOUS: In eukaryotes there are two forms of the enzymes: a
CC cytosolic one and a mitochondrial one. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the SHMT family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF237702; AAK15040.1; -; mRNA.
DR EMBL; AL596215; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC026055; AAH26055.1; -; mRNA.
DR EMBL; X94478; CAA64225.1; -; mRNA.
DR EMBL; X94479; CAA64226.1; -; mRNA.
DR CCDS; CCDS24799.1; -.
DR PIR; JC4959; JC4959.
DR RefSeq; NP_033197.2; NM_009171.2.
DR RefSeq; XP_006532707.1; XM_006532644.3.
DR PDB; 1EJI; X-ray; 2.90 A; A/B/C/D=1-478.
DR PDBsum; 1EJI; -.
DR AlphaFoldDB; P50431; -.
DR SMR; P50431; -.
DR BioGRID; 203222; 11.
DR STRING; 10090.ENSMUSP00000018744; -.
DR ChEMBL; CHEMBL4396; -.
DR iPTMnet; P50431; -.
DR PhosphoSitePlus; P50431; -.
DR SwissPalm; P50431; -.
DR REPRODUCTION-2DPAGE; P50431; -.
DR SWISS-2DPAGE; P50431; -.
DR EPD; P50431; -.
DR jPOST; P50431; -.
DR MaxQB; P50431; -.
DR PaxDb; P50431; -.
DR PeptideAtlas; P50431; -.
DR PRIDE; P50431; -.
DR ProteomicsDB; 263377; -.
DR Antibodypedia; 13529; 282 antibodies from 34 providers.
DR DNASU; 20425; -.
DR Ensembl; ENSMUST00000018744; ENSMUSP00000018744; ENSMUSG00000020534.
DR GeneID; 20425; -.
DR KEGG; mmu:20425; -.
DR UCSC; uc007jgo.1; mouse.
DR CTD; 6470; -.
DR MGI; MGI:98299; Shmt1.
DR VEuPathDB; HostDB:ENSMUSG00000020534; -.
DR eggNOG; KOG2467; Eukaryota.
DR GeneTree; ENSGT00390000002762; -.
DR HOGENOM; CLU_022477_0_0_1; -.
DR InParanoid; P50431; -.
DR OMA; VTNRNAI; -.
DR OrthoDB; 372408at2759; -.
DR PhylomeDB; P50431; -.
DR TreeFam; TF314667; -.
DR Reactome; R-MMU-196757; Metabolism of folate and pterines.
DR Reactome; R-MMU-71262; Carnitine synthesis.
DR UniPathway; UPA00193; -.
DR BioGRID-ORCS; 20425; 3 hits in 75 CRISPR screens.
DR ChiTaRS; Shmt1; mouse.
DR EvolutionaryTrace; P50431; -.
DR PRO; PR:P50431; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; P50431; protein.
DR Bgee; ENSMUSG00000020534; Expressed in yolk sac and 263 other tissues.
DR ExpressionAtlas; P50431; baseline and differential.
DR Genevisible; P50431; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0016597; F:amino acid binding; ISO:MGI.
DR GO; GO:0004372; F:glycine hydroxymethyltransferase activity; IMP:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0008732; F:L-allo-threonine aldolase activity; ISO:MGI.
DR GO; GO:0048027; F:mRNA 5'-UTR binding; ISO:MGI.
DR GO; GO:0000900; F:mRNA regulatory element binding translation repressor activity; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0030170; F:pyridoxal phosphate binding; ISS:UniProtKB.
DR GO; GO:0070905; F:serine binding; ISO:MGI.
DR GO; GO:0036094; F:small molecule binding; ISO:MGI.
DR GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEP:MGI.
DR GO; GO:1904482; P:cellular response to tetrahydrofolate; ISO:MGI.
DR GO; GO:0006231; P:dTMP biosynthetic process; IMP:BHF-UCL.
DR GO; GO:0046655; P:folic acid metabolic process; ISO:MGI.
DR GO; GO:0006545; P:glycine biosynthetic process; ISO:MGI.
DR GO; GO:0019264; P:glycine biosynthetic process from serine; ISO:MGI.
DR GO; GO:0006544; P:glycine metabolic process; ISS:UniProtKB.
DR GO; GO:0006565; P:L-serine catabolic process; ISO:MGI.
DR GO; GO:0006563; P:L-serine metabolic process; ISS:UniProtKB.
DR GO; GO:0017148; P:negative regulation of translation; ISO:MGI.
DR GO; GO:0006730; P:one-carbon metabolic process; IBA:GO_Central.
DR GO; GO:0051289; P:protein homotetramerization; ISS:UniProtKB.
DR GO; GO:0009113; P:purine nucleobase biosynthetic process; ISO:MGI.
DR GO; GO:0035999; P:tetrahydrofolate interconversion; IMP:MGI.
DR GO; GO:0046653; P:tetrahydrofolate metabolic process; ISS:UniProtKB.
DR CDD; cd00378; SHMT; 1.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR HAMAP; MF_00051; SHMT; 1.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR InterPro; IPR001085; Ser_HO-MeTrfase.
DR InterPro; IPR019798; Ser_HO-MeTrfase_PLP_BS.
DR InterPro; IPR039429; SHMT-like_dom.
DR PANTHER; PTHR11680; PTHR11680; 1.
DR Pfam; PF00464; SHMT; 1.
DR PIRSF; PIRSF000412; SHMT; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR PROSITE; PS00096; SHMT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; One-carbon metabolism;
KW Pyridoxal phosphate; Reference proteome; Transferase.
FT CHAIN 1..478
FT /note="Serine hydroxymethyltransferase, cytosolic"
FT /id="PRO_0000113505"
FT MOD_RES 251
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000269|PubMed:11063567"
FT CONFLICT 62
FT /note="C -> S (in Ref. 1; AAK15040 and 4; CAA64225/
FT CAA64226)"
FT /evidence="ECO:0000305"
FT CONFLICT 267..309
FT /note="VRSVDPKTGKETYYELESLINSAVFPGLQGGPHNHAIAGVAVA -> KFPYA
FT GTDSVGSHFLCGRDWENSGLSLLGKIGALALEELLRKK (in Ref. 4;
FT CAA64225)"
FT /evidence="ECO:0000305"
FT CONFLICT 304
FT /note="A -> R (in Ref. 4; CAA64226)"
FT /evidence="ECO:0000305"
FT STRAND 3..5
FT /evidence="ECO:0007829|PDB:1EJI"
FT HELIX 6..15
FT /evidence="ECO:0007829|PDB:1EJI"
FT HELIX 20..23
FT /evidence="ECO:0007829|PDB:1EJI"
FT HELIX 25..39
FT /evidence="ECO:0007829|PDB:1EJI"
FT STRAND 40..43
FT /evidence="ECO:0007829|PDB:1EJI"
FT HELIX 53..59
FT /evidence="ECO:0007829|PDB:1EJI"
FT HELIX 62..65
FT /evidence="ECO:0007829|PDB:1EJI"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:1EJI"
FT STRAND 76..78
FT /evidence="ECO:0007829|PDB:1EJI"
FT HELIX 81..97
FT /evidence="ECO:0007829|PDB:1EJI"
FT TURN 102..104
FT /evidence="ECO:0007829|PDB:1EJI"
FT STRAND 105..108
FT /evidence="ECO:0007829|PDB:1EJI"
FT HELIX 114..125
FT /evidence="ECO:0007829|PDB:1EJI"
FT STRAND 131..135
FT /evidence="ECO:0007829|PDB:1EJI"
FT HELIX 137..139
FT /evidence="ECO:0007829|PDB:1EJI"
FT HELIX 143..145
FT /evidence="ECO:0007829|PDB:1EJI"
FT HELIX 156..160
FT /evidence="ECO:0007829|PDB:1EJI"
FT STRAND 161..166
FT /evidence="ECO:0007829|PDB:1EJI"
FT TURN 170..172
FT /evidence="ECO:0007829|PDB:1EJI"
FT HELIX 177..187
FT /evidence="ECO:0007829|PDB:1EJI"
FT STRAND 190..194
FT /evidence="ECO:0007829|PDB:1EJI"
FT HELIX 205..214
FT /evidence="ECO:0007829|PDB:1EJI"
FT STRAND 218..222
FT /evidence="ECO:0007829|PDB:1EJI"
FT HELIX 224..226
FT /evidence="ECO:0007829|PDB:1EJI"
FT HELIX 227..231
FT /evidence="ECO:0007829|PDB:1EJI"
FT HELIX 238..240
FT /evidence="ECO:0007829|PDB:1EJI"
FT STRAND 243..250
FT /evidence="ECO:0007829|PDB:1EJI"
FT HELIX 251..253
FT /evidence="ECO:0007829|PDB:1EJI"
FT STRAND 259..264
FT /evidence="ECO:0007829|PDB:1EJI"
FT STRAND 266..270
FT /evidence="ECO:0007829|PDB:1EJI"
FT STRAND 277..280
FT /evidence="ECO:0007829|PDB:1EJI"
FT HELIX 282..290
FT /evidence="ECO:0007829|PDB:1EJI"
FT TURN 291..294
FT /evidence="ECO:0007829|PDB:1EJI"
FT HELIX 300..313
FT /evidence="ECO:0007829|PDB:1EJI"
FT HELIX 316..338
FT /evidence="ECO:0007829|PDB:1EJI"
FT STRAND 349..356
FT /evidence="ECO:0007829|PDB:1EJI"
FT HELIX 357..360
FT /evidence="ECO:0007829|PDB:1EJI"
FT HELIX 364..373
FT /evidence="ECO:0007829|PDB:1EJI"
FT STRAND 384..387
FT /evidence="ECO:0007829|PDB:1EJI"
FT STRAND 393..398
FT /evidence="ECO:0007829|PDB:1EJI"
FT HELIX 400..403
FT /evidence="ECO:0007829|PDB:1EJI"
FT TURN 404..406
FT /evidence="ECO:0007829|PDB:1EJI"
FT HELIX 409..431
FT /evidence="ECO:0007829|PDB:1EJI"
FT HELIX 439..447
FT /evidence="ECO:0007829|PDB:1EJI"
FT HELIX 453..467
FT /evidence="ECO:0007829|PDB:1EJI"
FT STRAND 474..476
FT /evidence="ECO:0007829|PDB:1EJI"
SQ SEQUENCE 478 AA; 52601 MW; 780C764C5AA3CEA3 CRC64;
MADRDATLWA SHEKMLSQPL KDSDAEVYSI IKKESNRQRV GLELIASENF ASRAVLEALG
SCLNNKYSEG YPGQRYYGGT EFIDELEMLC QKRALQAYHL DPQCWGVNVQ PYSGSPANFA
VYTALVEPHG RIMGLDLPDG GHLTHGFMTD KKKISATSIF FESMPYKVYP ETGYINYDQL
EENASLFHPK LIIAGTSCYS RNLDYARLRK IADDNGAYLM ADMAHISGLV AAGVVPSPFE
HCHVVTTTTH KTLRGCRAGM IFYRKGVRSV DPKTGKETYY ELESLINSAV FPGLQGGPHN
HAIAGVAVAL KQAMTTEFKI YQLQVLANCR ALSDALTELG YKIVTGGSDN HLILMDLRSK
GTDGGRAEKV LEACSIACNK NTCPGDKSAL RPSGLRLGTP ALTSRGLLEE DFQKVAHFIH
RGIELTLQIQ SHMATKATLK EFKEKLAGDE KIQSAVATLR EEVENFASNF SLPGLPDF
